Zhang Hui, Kong Lili, Li Jinhui, Liu Zhihan, Zhao Yiting, Lv Xiuyi, Wu Liangpei, Chai Lin, You Hongjie, Jin Jiabei, Cao Xinyi, Zheng Zhong, Liu Yadong, Yan Zejun, Jin Xiaofeng
Department of Urology, The First Affiliated Hospital of Ningbo University, Ningbo, Zhejiang, China.
Department of Biochemistry and Molecular Biology, Health Science Center, Ningbo University, Ningbo, Zhejiang, China.
JCI Insight. 2025 Apr 22;10(8). doi: 10.1172/jci.insight.186871.
It is well documented that impaired DNA damage repair (DDR) induces genomic instability that can efficiently increase the sensitivity of prostate cancer (PCa) cells to PARP inhibitors; however, the underlying mechanism remains elusive. Here, we found profound genomic instability in PCa cells with SPOP gene mutations and confirmed the sensitivity of SPOP-mutated PCa cells to olaparib-induced apoptosis. Mechanistically, we identified olaparib-induced CK2-mediated phosphorylation of PIAS1-S468, which in turn mediated SUMOylation of SPOP, thus promoting its E3 ligase activity in the DDR. Moreover, an abnormal CK2/PIAS1/SPOP axis due to SPOP mutations or defects in CK2-mediated phosphorylation of PIAS1, as well as SPOP inhibitor treatment, led to impaired DDR, thus increasing olaparib-induced apoptosis of PCa cells and enhancing olaparib sensitivity in animal models and patient-derived organoids. This suggested that disruption of the CK2/PIAS1/SPOP signaling axis could serve as an indicator for targeted therapy of PCa using a PARP inhibitor.
有充分文献记载,受损的DNA损伤修复(DDR)会诱发基因组不稳定,进而有效提高前列腺癌细胞(PCa)对PARP抑制剂的敏感性;然而,其潜在机制仍不清楚。在此,我们发现携带SPOP基因突变的PCa细胞存在严重的基因组不稳定,并证实SPOP突变的PCa细胞对奥拉帕尼诱导的凋亡敏感。从机制上讲,我们确定奥拉帕尼诱导CK2介导PIAS1-S468磷酸化,进而介导SPOP的SUMO化,从而促进其在DDR中的E3连接酶活性。此外,由于SPOP突变或CK2介导的PIAS1磷酸化缺陷导致的异常CK2/PIAS1/SPOP轴,以及SPOP抑制剂处理,都会导致DDR受损,从而增加奥拉帕尼诱导的PCa细胞凋亡,并增强动物模型和患者来源类器官对奥拉帕尼的敏感性。这表明CK2/PIAS1/SPOP信号轴的破坏可作为使用PARP抑制剂对PCa进行靶向治疗的指标。